Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA
Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA
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SACLA 使用 X 射线自由电子激光辐射对金属蛋白进行时间分辨研究
DOI：
10.1016/j.bbagen.2019.129466
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Sugimoto Hiroshi
中科院分区：
文献类型：
--
作者：
Suga Michihiro;Shimada Atsuhiro;Akita Fusamichi;Shen Jian-Ren;Tosha Takehiko;Sugimoto Hiroshi
背景X射线自由电子激光（XFEL）的发明为结构生物学提供了前所未有的新机遇。XFEL的优点是X射线的强脉冲和非常短的脉冲持续时间（<10 fs），有望成为无损伤和时间分辨的晶体学方法。具体来说，金属蛋白参与的生物能源转换的基本反应，包括光系统II，细胞色素氧化酶和一氧化氮reductase.Major conclusionsXFEL与泵探测技术成功地可视化的反应过程和动力学的蛋白质。由于金属蛋白的活性中心对X射线辐射非常敏感，因此通过XFEL获得的无损伤结构对于得出机理性结论至关重要。样品传输和反应引发的方法和工具是成功测量时间分辨数据的关键。一般意义XFEL是深入了解结构动力学和生物大分子催化反应的复杂机制的方法的中心。时间分辨X射线晶体学的应用得到了进一步的发展。这篇文章是一个特殊问题的一部分，题为新的测量技术可视化'活'蛋白质分子。
BackgroundThe invention of the X-ray free-electron laser (XFEL) has provided unprecedented new opportunities for structural biology. The advantage of XFEL is an intense pulse of X-rays and a very short pulse duration (<10 fs) promising a damage-free and time-resolved crystallography approach.Scope of reviewRecent time-resolved crystallographic analyses in XFEL facility SACLA are reviewed. Specifically, metalloproteins involved in the essential reactions of bioenergy conversion including photosystem II, cytochromecoxidase and nitric oxide reductase are described.Major conclusionsXFEL with pump-probe techniques successfully visualized the process of the reaction and the dynamics of a protein. Since the active center of metalloproteins is very sensitive to the X-ray radiation, damage-free structures obtained by XFEL are essential to draw mechanistic conclusions. Methods and tools for sample delivery and reaction initiation are key for successful measurement of the time-resolved data.General significanceXFEL is at the center of approaches to gain insight into complex mechanism of structural dynamics and the reactions catalyzed by biological macromolecules. Further development has been carried out to expand the application of time-resolved X-ray crystallography. This article is part of a Special Issue entitled Novel measurement techniques for visualizing ‘live’ protein molecules.